coagulation factor XII isoform X1 [Homo sapiens]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| Tryp_SPc | cd00190 | Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
261-500 | 1.12e-91 | |||||
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues. : Pssm-ID: 238113 [Multi-domain] Cd Length: 232 Bit Score: 279.16 E-value: 1.12e-91
|
|||||||||
| Kringle | pfam00051 | Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ... |
105-183 | 3.55e-28 | |||||
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, prothrombin, and apolipoprotein A. Structure is disulfide-rich, nearly all-beta. : Pssm-ID: 395005 Cd Length: 79 Bit Score: 107.01 E-value: 3.55e-28
|
|||||||||
| FN1 | cd00061 | Fibronectin type 1 domain, approximately 40 residue long with two conserved disulfide bridges. ... |
21-61 | 3.30e-09 | |||||
Fibronectin type 1 domain, approximately 40 residue long with two conserved disulfide bridges. FN1 is one of three types of internal repeats which combine to form larger domains within fibronectin. Fibronectin, a plasma protein that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin, usually exists as a dimer in plasma and as an insoluble multimer in extracellular matrices. Dimers of nearly identical subunits are linked by a disulfide bond close to their C-terminus. FN1 domains also found in coagulation factor XII, HGF activator, and tissue-type plasminogen activator. In tissue plasminogen activator, FN1 domains may form functional fibrin-binding units with EGF-like domains C-terminal to FN1. : Pssm-ID: 238018 Cd Length: 43 Bit Score: 52.33 E-value: 3.30e-09
|
|||||||||
| EGF | pfam00008 | EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ... |
66-94 | 2.57e-06 | |||||
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains. : Pssm-ID: 394967 Cd Length: 31 Bit Score: 43.91 E-value: 2.57e-06
|
|||||||||
| Name | Accession | Description | Interval | E-value | |||||
| Tryp_SPc | cd00190 | Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
261-500 | 1.12e-91 | |||||
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues. Pssm-ID: 238113 [Multi-domain] Cd Length: 232 Bit Score: 279.16 E-value: 1.12e-91
|
|||||||||
| Tryp_SPc | smart00020 | Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
260-497 | 5.93e-91 | |||||
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues. Pssm-ID: 214473 Cd Length: 229 Bit Score: 276.87 E-value: 5.93e-91
|
|||||||||
| Trypsin | pfam00089 | Trypsin; |
261-497 | 1.72e-67 | |||||
Trypsin; Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 216.15 E-value: 1.72e-67
|
|||||||||
| COG5640 | COG5640 | Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
259-501 | 3.19e-64 | |||||
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 209.12 E-value: 3.19e-64
|
|||||||||
| Kringle | pfam00051 | Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ... |
105-183 | 3.55e-28 | |||||
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, prothrombin, and apolipoprotein A. Structure is disulfide-rich, nearly all-beta. Pssm-ID: 395005 Cd Length: 79 Bit Score: 107.01 E-value: 3.55e-28
|
|||||||||
| KR | cd00108 | Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ... |
103-183 | 7.74e-24 | |||||
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as peptides, other proteins, membranes, or phospholipids. They are autonomous structural domains, found in a varying number of copies, in blood clotting and fibrinolytic proteins, some serine proteases and plasma proteins. Plasminogen-like kringles possess affinity for free lysine and lysine-containing peptides. Pssm-ID: 238056 Cd Length: 83 Bit Score: 95.14 E-value: 7.74e-24
|
|||||||||
| KR | smart00130 | Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ... |
105-183 | 1.11e-23 | |||||
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides. Pssm-ID: 214527 Cd Length: 83 Bit Score: 94.76 E-value: 1.11e-23
|
|||||||||
| FN1 | cd00061 | Fibronectin type 1 domain, approximately 40 residue long with two conserved disulfide bridges. ... |
21-61 | 3.30e-09 | |||||
Fibronectin type 1 domain, approximately 40 residue long with two conserved disulfide bridges. FN1 is one of three types of internal repeats which combine to form larger domains within fibronectin. Fibronectin, a plasma protein that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin, usually exists as a dimer in plasma and as an insoluble multimer in extracellular matrices. Dimers of nearly identical subunits are linked by a disulfide bond close to their C-terminus. FN1 domains also found in coagulation factor XII, HGF activator, and tissue-type plasminogen activator. In tissue plasminogen activator, FN1 domains may form functional fibrin-binding units with EGF-like domains C-terminal to FN1. Pssm-ID: 238018 Cd Length: 43 Bit Score: 52.33 E-value: 3.30e-09
|
|||||||||
| fn1 | pfam00039 | Fibronectin type I domain; |
23-58 | 1.40e-06 | |||||
Fibronectin type I domain; Pssm-ID: 459644 Cd Length: 40 Bit Score: 45.00 E-value: 1.40e-06
|
|||||||||
| EGF | pfam00008 | EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ... |
66-94 | 2.57e-06 | |||||
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains. Pssm-ID: 394967 Cd Length: 31 Bit Score: 43.91 E-value: 2.57e-06
|
|||||||||
| EGF_CA | cd00054 | Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ... |
69-97 | 1.10e-03 | |||||
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements. Pssm-ID: 238011 Cd Length: 38 Bit Score: 36.46 E-value: 1.10e-03
|
|||||||||
| FN1 | smart00058 | Fibronectin type 1 domain; One of three types of internal repeat within the plasma protein, ... |
23-63 | 2.08e-03 | |||||
Fibronectin type 1 domain; One of three types of internal repeat within the plasma protein, fibronectin. Found also in coagulation factor XII, HGF activator and tissue-type plasminogen activator. In t-PA and fibronectin, this domain type contributes to fibrin-binding. Pssm-ID: 214494 Cd Length: 45 Bit Score: 36.17 E-value: 2.08e-03
|
|||||||||
| Name | Accession | Description | Interval | E-value | |||||
| Tryp_SPc | cd00190 | Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ... |
261-500 | 1.12e-91 | |||||
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues. Pssm-ID: 238113 [Multi-domain] Cd Length: 232 Bit Score: 279.16 E-value: 1.12e-91
|
|||||||||
| Tryp_SPc | smart00020 | Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ... |
260-497 | 5.93e-91 | |||||
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues. Pssm-ID: 214473 Cd Length: 229 Bit Score: 276.87 E-value: 5.93e-91
|
|||||||||
| Trypsin | pfam00089 | Trypsin; |
261-497 | 1.72e-67 | |||||
Trypsin; Pssm-ID: 459667 [Multi-domain] Cd Length: 219 Bit Score: 216.15 E-value: 1.72e-67
|
|||||||||
| COG5640 | COG5640 | Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ... |
259-501 | 3.19e-64 | |||||
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 444365 [Multi-domain] Cd Length: 262 Bit Score: 209.12 E-value: 3.19e-64
|
|||||||||
| Kringle | pfam00051 | Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ... |
105-183 | 3.55e-28 | |||||
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, prothrombin, and apolipoprotein A. Structure is disulfide-rich, nearly all-beta. Pssm-ID: 395005 Cd Length: 79 Bit Score: 107.01 E-value: 3.55e-28
|
|||||||||
| KR | cd00108 | Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ... |
103-183 | 7.74e-24 | |||||
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as peptides, other proteins, membranes, or phospholipids. They are autonomous structural domains, found in a varying number of copies, in blood clotting and fibrinolytic proteins, some serine proteases and plasma proteins. Plasminogen-like kringles possess affinity for free lysine and lysine-containing peptides. Pssm-ID: 238056 Cd Length: 83 Bit Score: 95.14 E-value: 7.74e-24
|
|||||||||
| KR | smart00130 | Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ... |
105-183 | 1.11e-23 | |||||
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides. Pssm-ID: 214527 Cd Length: 83 Bit Score: 94.76 E-value: 1.11e-23
|
|||||||||
| eMpr | COG3591 | V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ... |
281-487 | 1.16e-09 | |||||
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 442810 [Multi-domain] Cd Length: 194 Bit Score: 57.76 E-value: 1.16e-09
|
|||||||||
| FN1 | cd00061 | Fibronectin type 1 domain, approximately 40 residue long with two conserved disulfide bridges. ... |
21-61 | 3.30e-09 | |||||
Fibronectin type 1 domain, approximately 40 residue long with two conserved disulfide bridges. FN1 is one of three types of internal repeats which combine to form larger domains within fibronectin. Fibronectin, a plasma protein that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin, usually exists as a dimer in plasma and as an insoluble multimer in extracellular matrices. Dimers of nearly identical subunits are linked by a disulfide bond close to their C-terminus. FN1 domains also found in coagulation factor XII, HGF activator, and tissue-type plasminogen activator. In tissue plasminogen activator, FN1 domains may form functional fibrin-binding units with EGF-like domains C-terminal to FN1. Pssm-ID: 238018 Cd Length: 43 Bit Score: 52.33 E-value: 3.30e-09
|
|||||||||
| fn1 | pfam00039 | Fibronectin type I domain; |
23-58 | 1.40e-06 | |||||
Fibronectin type I domain; Pssm-ID: 459644 Cd Length: 40 Bit Score: 45.00 E-value: 1.40e-06
|
|||||||||
| EGF | pfam00008 | EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ... |
66-94 | 2.57e-06 | |||||
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains. Pssm-ID: 394967 Cd Length: 31 Bit Score: 43.91 E-value: 2.57e-06
|
|||||||||
| alphaLP-like | cd21112 | alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and ... |
444-496 | 5.71e-04 | |||||
alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and similar proteins; This family represents the catalytic domain of alpha-lytic protease (alpha-LP) and its closely-related homologs. Alpha-lytic protease (EC 3.4.21.12; also called alpha-lytic endopeptidase), originally isolated from the myxobacterium Lysobacter enzymogenes, belongs to the MEROPS peptidase family S1, subfamily S1E (streptogrisin A subfamily). It is synthesized as a pro-enzyme, thus having two domains; the N-terminal pro-domain acts as a foldase, required transiently for the correct folding of the protease domain, and also acts as a potent inhibitor of the mature enzyme, while the C-terminal domain catalyzes the cleavage of peptide bonds. Members of the alpha-lytic protease subfamily include Nocardiopsis alba protease (NAPase), a secreted chymotrypsin from the alkaliphile Cellulomonas bogoriensis, streptogrisins (SPG-A, SPG-B, SPG-C, and SPG-D), and Thermobifida fusca protease A (TFPA). These serine proteases have characteristic kinetic stability, exhibited by their extremely slow unfolding kinetics. The active site, characteristic of serine proteases, contains the catalytic triad consisting of serine acting as a nucleophile, aspartate as an electrophile, and histidine as a base, all required for activity. This model represents the C-terminal catalytic domain of alpha-lytic proteases. Pssm-ID: 411050 Cd Length: 188 Bit Score: 41.14 E-value: 5.71e-04
|
|||||||||
| EGF_CA | cd00054 | Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ... |
69-97 | 1.10e-03 | |||||
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements. Pssm-ID: 238011 Cd Length: 38 Bit Score: 36.46 E-value: 1.10e-03
|
|||||||||
| FN1 | smart00058 | Fibronectin type 1 domain; One of three types of internal repeat within the plasma protein, ... |
23-63 | 2.08e-03 | |||||
Fibronectin type 1 domain; One of three types of internal repeat within the plasma protein, fibronectin. Found also in coagulation factor XII, HGF activator and tissue-type plasminogen activator. In t-PA and fibronectin, this domain type contributes to fibrin-binding. Pssm-ID: 214494 Cd Length: 45 Bit Score: 36.17 E-value: 2.08e-03
|
|||||||||
| EGF | cd00053 | Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ... |
69-96 | 6.77e-03 | |||||
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium. Pssm-ID: 238010 Cd Length: 36 Bit Score: 34.37 E-value: 6.77e-03
|
|||||||||
| Blast search parameters | ||||
|
